Prion-like Domains in Eukaryotic Viruses

Human Microbiology Institute have discovered prion-like domains in thousands of viruses, bolstering research that opens new ways of viral pathogenicity, suggests new targets for development of new antiviral drugs and links viruses to diseases such as Alzheimer’s and Parkinson’s.

Prions are proteins that can self-propagate, leading to the misfolding of proteins. In addition to the previously demonstrated pathogenic roles of prions during the development of different mammalian diseases, including neurodegenerative diseases, they have recently been shown to represent an important functional component in many prokaryotic and eukaryotic organisms and bacteriophages, confirming the previously unexplored important regulatory and functional roles.

Prions are infectious proteins that due to their β-sheet-rich conformation can self-propagate, leading to the accumulation of misfolded proteins in the brain possesses neurotoxic effects and are known to be implicated in neurodegenerative diseases. The reason for the human prions formation remains illusive.

In the paper, HMI discusses the discovery of over 2,600 proteins possessing prion-like structures across viruses.

The discovery of prions in viral proteins uncovers a previously unknown pathway for the development of diseases associated with protein misfolding, including Alzheimer’s and Parkinson’s diseases, ataxias and amyotrophic lateral sclerosis

Previous works have shown that viruses play a role in the development of some diseases listed above, and the discovery by HMI for the first time proposes that the misfolding of proteins is the previously unknown pathway for these prions to infect humans.

Moreover, the research suggests a new possible targets that can be used for the development of novel antiviral drugs, which could have huge implications in how we treat and fight a whole host of diseases.

In another aspect , this study explains the previously unknown mechanisms of viral pathogenicity

The research, was published in Nature’s Scientific Reports.

Prion-Like Domains in Eukaryotic Viruses / Scientific Reports (2018)

Scientific Reports (2018)

Prion-Like Domains in Eukaryotic Viruses

Publication Type

Journal article

Authors

George V. Tetz

Victor Tetz

Abstract

Prions are proteins that can self-propagate, leading to the misfolding of proteins. In addition to the previously demonstrated pathogenic roles of prions during the development of different mammalian diseases, including neurodegenerative diseases, they have recently been shown to represent an important functional component in many prokaryotic and eukaryotic organisms and bacteriophages, confirming the previously unexplored important regulatory and functional roles. However, an in-depth analysis of these domains in eukaryotic viruses has not been performed. Here, we examined the presence of prion-like proteins in eukaryotic viruses that play a primary role in different ecosystems and that are associated with emerging diseases in humans. We identified relevant functional associations in different viral processes and regularities in their presence at different taxonomic levels. Using the prion-like amino-acid composition computational algorithm, we detected 2679 unique putative prion-like domains within 2,742,160 publicly available viral protein sequences. Our findings indicate that viral prion-like proteins can be found in different viruses of insects, plants, mammals, and humans. The analysis performed here demonstrated common patterns in the distribution of prion-like domains across viral orders and families, and revealed probable functional associations with different steps of viral replication and interaction with host cells. These data allow the identification of the viral prion-like proteins as potential novel regulators of viral infections.